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Bdellovibrio bacteriovorus phosphoglucose isomerase structures reveal novel rigidity in the active site of a selected subset of enzymes upon substrate binding
Open Biology ( IF 5.8 ) Pub Date : 2021-08-11 , DOI: 10.1098/rsob.210098
R W Meek 1 , I T Cadby 2 , A L Lovering 2
Affiliation  

Glycolysis and gluconeogenesis are central pathways of metabolism across all domains of life. A prominent enzyme in these pathways is phosphoglucose isomerase (PGI), which mediates the interconversion of glucose-6-phosphate and fructose-6-phosphate. The predatory bacterium Bdellovibrio bacteriovorus leads a complex life cycle, switching between intraperiplasmic replicative and extracellular ‘hunter’ attack-phase stages. Passage through this complex life cycle involves different metabolic states. Here we present the unliganded and substrate-bound structures of the B. bacteriovorus PGI, solved to 1.74 Å and 1.67 Å, respectively. These structures reveal that an induced-fit conformational change within the active site is not a prerequisite for the binding of substrates in some PGIs. Crucially, we suggest a phenylalanine residue, conserved across most PGI enzymes but substituted for glycine in B. bacteriovorus and other select organisms, is central to the induced-fit mode of substrate recognition for PGIs. This enzyme also represents the smallest conventional PGI characterized to date and probably represents the minimal requirements for a functional PGI.



中文翻译:

Bdellovibrio bacteriovorus 磷酸葡萄糖异构酶结构揭示了在底物结合时选定酶子集的活性位点的新刚性

糖酵解和糖异生是生命各个领域代谢的中心途径。这些途径中的一个重要酶是磷酸葡萄糖异构酶 (PGI),它介导 6-磷酸葡萄糖和 6-磷酸果糖的相互转化。捕食性细菌Bdellovibrio bacteriovorus导致复杂的生命周期,在周质内复制和细胞外“猎人”攻击阶段之间切换。通过这个复杂的生命周期涉及不同的代谢状态。在这里,我们展示了B. bacteriovorus的未配体和底物结合结构PGI,分别解析为 1.74 Å 和 1.67 Å。这些结构表明,活性位点内的诱导拟合构象变化不是某些 PGI 中底物结合的先决条件。至关重要的是,我们建议苯丙氨酸残基,在大多数 PGI 酶中保守,但在B. bacteriovorus和其他选择的生物体中取代甘氨酸,是 PGI 底物识别的诱导拟合模式的核心。这种酶也代表了迄今为止表征的最小的常规 PGI,并且可能代表了对功能性 PGI 的最低要求。

更新日期:2021-08-11
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